CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011166
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase SIZ1 
Protein Synonyms/Alias
 SAP and Miz-finger domain-containing protein 1; Ubiquitin-like protein ligase 1 
Gene Name
 SIZ1 
Gene Synonyms/Alias
 ULL1; YDR409W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
213SAKFKLSKADYNLLSubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Acts as an E3 ligase mediating SUMO/Smt3 attachment to septins and PCNA. May be involved in chromosome maintenance. 
Sequence Annotation
 DOMAIN 34 68 SAP.
 DOMAIN 162 314 PINIT.
 ZN_FING 346 423 SP-RING-type.
 REGION 794 904 Required for localization at the bud
 MOD_RES 132 132 Phosphoserine.
 MOD_RES 794 794 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 904 AA 
Protein Sequence
MINLEDYWED ETPGPDREPT NELRNEVEET ITLMELLKVS ELKDICRSVS FPVSGRKAVL 60
QDLIRNFLQN ALVVGKSDPY RVQAVKFLIE RIRKNEPLPV YKDLWNALRK GTPLSAITVR 120
SMEGPPTVQQ QSPSVIRQSP TQRRKTSTTS STSRAPPPTN PDASSSSSSF AVPTIHFKES 180
PFYKIQRLIP ELVMNVEVTG GRGMCSAKFK LSKADYNLLS NPNSKHRLYL FSGMINPLGS 240
RGNEPIQFPF PNELRCNNVQ IKDNIRGFKS KPGTAKPADL TPHLKPYTQQ NNVELIYAFT 300
TKEYKLFGYI VEMITPEQLL EKVLQHPKII KQATLLYLKK TLREDEEMGL TTTSTIMSLQ 360
CPISYTRMKY PSKSINCKHL QCFDALWFLH SQLQIPTWQC PVCQIDIALE NLAISEFVDD 420
ILQNCQKNVE QVELTSDGKW TAILEDDDDS DSDSNDGSRS PEKGTSVSDH HCSSSHPSEP 480
IIINLDSDDD EPNGNNPHVT NNHDDSNRHS NDNNNNSIKN NDSHNKNNNN NNNNNNNNND 540
NNNSIENNDS NSNNKHDHGS RSNTPSHNHT KNLMNDNDDD DDDRLMAEIT SNHLKSTNTD 600
ILTEKGSSAP SRTLDPKSYN IVASETTTPV TNRVIPEYLG NSSSYIGKQL PNILGKTPLN 660
VTAVDNSSHL ISPDVSVSSP TPRNTASNAS SSALSTPPLI RMSSLDPRGS TVPDKTIRPP 720
INSNSYTASI SDSFVQPQES SVFPPREQNM DMSFPSTVNS RFNDPRLNTT RFPDSTLRGA 780
TILSNNGLDQ RNNSLPTTEA ITRNDVGRQN STPVLPTLPQ NVPIRTNSNK SGLPLINNEN 840
SVPNPPNTAT IPLQKSRLIV NPFIPRRPYS NVLPQKRQLS NTSSTSPIMG TWKTQDYGKK 900
YNSG 904 
Gene Ontology
 GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0000790; C:nuclear chromatin; IDA:SGD.
 GO:0005940; C:septin ring; IDA:SGD.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0019789; F:SUMO ligase activity; IMP:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007059; P:chromosome segregation; IMP:SGD.
 GO:0016925; P:protein sumoylation; IMP:SGD. 
Interpro
 IPR023321; PINIT.
 IPR003034; SAP_dom.
 IPR027229; SIZ1/SIZ2/Pli1/Gei17.
 IPR004181; Znf_MIZ.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF14324; PINIT
 PF02037; SAP
 PF02891; zf-MIZ 
SMART
 SM00513; SAP 
PROSITE
 PS51466; PINIT
 PS50800; SAP
 PS51044; ZF_SP_RING 
PRINTS